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机构地区:[1]烟台大学化学院,烟台264005
出 处:《分析化学》2004年第5期615-618,共4页Chinese Journal of Analytical Chemistry
摘 要:用荧光光谱法、分光光度法研究了水溶液中秋水仙碱与牛血清白蛋白 (BSA)的相互结合反应。研究表明 :二者以摩尔比 1∶1牢固结合 ,其平衡常数K0 =1.92× 10 5L/mol。根据F rster非辐射能量转移机理 ,求算了给体 (BSA)与受体 (秋水仙碱 )间距离r =3.6 3nm和能量转移效率E =0 .17。实验表明The binding reaction between colchicine and bovine serum albumins (BSA) in aqueous solution was studied by fluorescence and ultraviolet-visibale absorption spectra. The results indicates that colchicine strongly binds to BSA with a molar ratio of 1:1 and the equilibrium constant K-0 is 1.92 x 10(5) L/mol. The Stern-Volmer curve on the fluorescence of BSA quenched by series of colchicine concentrations shows good linear relationship, which illustrates the combination reaction of colchicine and BSA is a single static quenching process. The shortest binding distance ( r = 3.63 nm) and energy transfer efficiency (E = 0.17) between donor (BSA) and acceptor (colchicine) were obtained by Foster's nonradiative energy transfer mechanism.
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